ID PAQR8_MOUSE Reviewed; 354 AA. AC Q80ZE5; Q3UHI5; Q8C891; Q8CCW9; Q9DA71; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 16-OCT-2019, entry version 113. DE RecName: Full=Membrane progestin receptor beta {ECO:0000250|UniProtKB:Q8TEZ7}; DE Short=mPR beta {ECO:0000250|UniProtKB:Q8TEZ7}; DE AltName: Full=Lysosomal membrane protein in brain 1 {ECO:0000303|PubMed:11676489}; DE AltName: Full=Membrane progesterone P4 receptor beta {ECO:0000250|UniProtKB:Q8TEZ7}; DE AltName: Full=Membrane progesterone receptor beta {ECO:0000250|UniProtKB:Q8TEZ7}; DE AltName: Full=Progesterone and adipoQ receptor family member 8; DE AltName: Full=Progestin and adipoQ receptor family member 8 {ECO:0000250|UniProtKB:Q8TEZ7}; DE AltName: Full=Progestin and adipoQ receptor family member VIII; GN Name=Paqr8 {ECO:0000312|MGI:MGI:1921479}; Synonyms=Mprb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=CD-1; TISSUE=Testis; RX PubMed=12601167; DOI=10.1073/pnas.0436133100; RA Zhu Y., Bond J., Thomas P.; RT "Identification, classification, and partial characterization of genes RT in humans and other vertebrates homologous to a fish membrane RT progestin receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2237-2242(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16044242; DOI=10.1007/s00239-004-0375-2; RA Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C., RA Funk W.D.; RT "PAQR proteins: a novel membrane receptor family defined by an ancient RT 7-transmembrane pass motif."; RL J. Mol. Evol. 61:372-380(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head, Medulla oblongata, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=11676489; DOI=10.1006/bbrc.2001.5825; RA Suzuki T., Ganesh S., Agarwala K.L., Morita R., Sugimoto Y., RA Inazawa J., Delgado-Escueta A.V., Yamakawa K.; RT "A novel gene in the chromosomal region for juvenile myoclonic RT epilepsy on 6p12 encodes a brain-specific lysosomal membrane RT protein."; RL Biochem. Biophys. Res. Commun. 288:626-636(2001). CC -!- FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G CC proteins. Seems to act through a G(i) mediated pathway (By CC similarity). May be involved in oocyte maturation CC (PubMed:12601167). Also binds dehydroepiandrosterone (DHEA), CC pregnanolone, pregnenolone and allopregnanolone (By similarity). CC {ECO:0000250|UniProtKB:Q8TEZ7, ECO:0000269|PubMed:12601167}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:Q8TEZ7}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalizes with a lysosomal protein CC CTSD/cathepsin D. {ECO:0000250|UniProtKB:Q8TEZ7}. CC -!- TISSUE SPECIFICITY: Expressed in brain and testis. CC {ECO:0000269|PubMed:11676489}. CC -!- MISCELLANEOUS: Non-classical progesterone receptors involved in CC extranuclear signaling are classified in 2 groups: the class II CC progestin and adipoQ receptor (PAQR) family (also called mPRs) CC (PAQR5, PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like CC heme/steroid-binding protein family (also called MAPRs) (PGRMC1, CC PGRMC2, NENF and CYB5D2). {ECO:0000250|UniProtKB:Q8TEZ7}. CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC27629.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF313617; AAO47230.1; -; mRNA. DR EMBL; AY424297; AAR08385.1; -; mRNA. DR EMBL; AK006107; BAB24412.1; -; mRNA. DR EMBL; AK029772; BAC26609.1; -; mRNA. DR EMBL; AK031969; BAC27629.1; ALT_FRAME; mRNA. DR EMBL; AK048045; BAC33221.1; -; mRNA. DR EMBL; AK147376; BAE27872.1; -; mRNA. DR EMBL; BC059813; AAH59813.1; -; mRNA. DR CCDS; CCDS14844.1; -. DR RefSeq; NP_083105.3; NM_028829.3. DR RefSeq; XP_006495640.1; XM_006495577.2. DR RefSeq; XP_006495641.1; XM_006495578.3. DR SMR; Q80ZE5; -. DR STRING; 10090.ENSMUSP00000141054; -. DR iPTMnet; Q80ZE5; -. DR PhosphoSitePlus; Q80ZE5; -. DR MaxQB; Q80ZE5; -. DR PaxDb; Q80ZE5; -. DR PRIDE; Q80ZE5; -. DR Ensembl; ENSMUST00000068880; ENSMUSP00000069127; ENSMUSG00000025931. DR Ensembl; ENSMUST00000167119; ENSMUSP00000128781; ENSMUSG00000025931. DR Ensembl; ENSMUST00000187651; ENSMUSP00000140913; ENSMUSG00000025931. DR Ensembl; ENSMUST00000189400; ENSMUSP00000141054; ENSMUSG00000025931. DR GeneID; 74229; -. DR KEGG; mmu:74229; -. DR UCSC; uc007ald.1; mouse. DR CTD; 85315; -. DR MGI; MGI:1921479; Paqr8. DR eggNOG; KOG0748; Eukaryota. DR eggNOG; COG1272; LUCA. DR GeneTree; ENSGT00940000159860; -. DR HOGENOM; HOG000230872; -. DR InParanoid; Q80ZE5; -. DR OMA; REPYIHA; -. DR OrthoDB; 1524940at2759; -. DR PhylomeDB; Q80ZE5; -. DR TreeFam; TF319738; -. DR ChiTaRS; Paqr8; mouse. DR PRO; PR:Q80ZE5; -. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000025931; Expressed in 198 organ(s), highest expression level in cerebellum. DR Genevisible; Q80ZE5; MM. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0005496; F:steroid binding; IBA:GO_Central. DR GO; GO:0003707; F:steroid hormone receptor activity; IBA:GO_Central. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW. DR GO; GO:0048545; P:response to steroid hormone; IBA:GO_Central. DR InterPro; IPR004254; AdipoR/HlyIII-related. DR PANTHER; PTHR20855; PTHR20855; 1. DR Pfam; PF03006; HlyIII; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Developmental protein; KW Differentiation; Lipid-binding; Membrane; Oogenesis; Receptor; KW Reference proteome; Steroid-binding; Transmembrane; KW Transmembrane helix. FT CHAIN 1 354 Membrane progestin receptor beta. FT /FTId=PRO_0000218841. FT TOPO_DOM 1 76 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 77 97 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 98 111 Extracellular. {ECO:0000255}. FT TRANSMEM 112 132 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 133 173 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 174 194 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 195 213 Extracellular. {ECO:0000255}. FT TRANSMEM 214 234 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 235 243 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 244 264 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 265 283 Extracellular. {ECO:0000255}. FT TRANSMEM 284 304 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 305 315 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 316 336 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 337 354 Extracellular. {ECO:0000255}. FT CONFLICT 41 41 D -> G (in Ref. 3; AAR08385/BAC33221). FT {ECO:0000305}. FT CONFLICT 116 116 I -> V (in Ref. 1; AAO47230). FT {ECO:0000305}. FT CONFLICT 177 177 I -> L (in Ref. 1; AAO47230). FT {ECO:0000305}. FT CONFLICT 339 339 T -> S (in Ref. 1; AAO47230). FT {ECO:0000305}. SQ SEQUENCE 354 AA; 40430 MW; 14544CBB3338B538 CRC64; MTTAILERLS TLSMSGQQLR RLPKILEEGL PKMPCTVPET DVPQLFREPY IHAGYRPTGH EWRYYFFSLF QKHNEVVNVW THLLAALAVL LRFWAFVEAG ALQWASPHTL PLLLFILSSI TYLTCSLLAH LLQSKSELSH YTFYFVDYVG VSVYQYGSAL AHFFYSSDQA WYELFWIFFL PAAAFCGWLS CAGCCYAKYR YRRPYPVMRK ICQVVPAGLA FVLDISPVAH RVALCHLAGC QEQAAWYHTL QILFFLVSAY FFSCPVPEKY FPGSCDIVGH GHQIFHAFLS VCTLSQLEAI LLDYQGRHEI FLQRHGPLSV YSACLSFFVL AACSAATATL LRHKVKDRLI KKDS //